Probing The Structural Network of Buried Water Molecules in the Hydrophobic core of Staphlococcal Nuclease
EMSL Project ID
13497
Abstract
We have crystallized and solved the X-ray crystallographic structures of a number of mutants of the Staphylococcal nuclease protein. These proteins contain a point mutation at a single site within the hydrophobic core. There are water molecules present in the cryogenic (-178 C) structures of the hydrophobic core of some of these mutants. We also have evidence of local unfolding via circular dichroism measurements.What I would like to do by FTIR is evaluate the effect of mutation on water structure within the hydrophobic core by FTIR spectral analysis of these mutant proteins. I am therefore interested in the spectral range 2700-4000 cm-1, and the protein fingerprint region 800-1800 cm-1 at cryo and room (25 C) temperature.
Project Details
Project type
Exploratory Research
Start Date
2005-02-14
End Date
2007-03-22
Status
Closed
Released Data Link
Team
Principal Investigator